Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation

Carlos Martinez-Fleites; Catarina I. P. D. Guerreiro; Martin J. Baumann; Edward J. Taylor; Jose A. M. Prates; Luis M. A. Ferreira; Carlos M. G. A. Fontes; Harry Brumer; Gideon J. Davies

doi:10.1074/jbc.M603583200

Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation

Carlos Martinez-Fleites, Catarina I. P. D. Guerreiro, Martin J. Baumann, Edward J. Taylor, Jose A. M. Prates, Luis M. A. Ferreira, Carlos M. G. A. Fontes, Harry Brumer, Gideon J. Davies

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The enzymatic degradation of the plant cell wall is central both to the natural carbon cycle and, increasingly, to environmentally friendly routes to biomass conversion, including the production of biofuels. The plant cell wall is a complex composite of cellulose microfibrils embedded in diverse polysaccharides collectively termed hemicelluloses. Xyloglucan is one such polysaccharide whose hydrolysis is catalyzed by diverse xyloglucanases. Here we present the structure of the Clostridium thermocellum xyloglucanase Xgh74A in both apo and ligand-complexed forms. The structures, in combination with mutagenesis data on the catalytic residues and the kinetics and specificity of xyloglucan hydrolysis reveal a complex subsite specificity accommodating seventeen monosaccharide moieties of the multibranched substrate in an open substrate binding terrain.

Original language	English
Pages (from-to)	24922-24933
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	281
Issue number	34
DOIs	https://doi.org/10.1074/jbc.M603583200
Publication status	Published - 25 Aug 2006

Keywords

END-SPECIFIC CELLOBIOHYDROLASE
PLANT-CELL WALL
GLYCOSYL HYDROLASES
CELLULOSE SURFACES
EXPRESSION
CLONING
CLASSIFICATION
ENDOGLUCANASE
BIOSYNTHESIS
PURIFICATION

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10.1074/jbc.M603583200

Cite this

Martinez-Fleites, C., Guerreiro, C. I. P. D., Baumann, M. J., Taylor, E. J., Prates, J. A. M., Ferreira, L. M. A., Fontes, C. M. G. A., Brumer, H., & Davies, G. J. (2006). Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation. Journal of Biological Chemistry, 281(34), 24922-24933. https://doi.org/10.1074/jbc.M603583200

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title = "Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation",

abstract = "The enzymatic degradation of the plant cell wall is central both to the natural carbon cycle and, increasingly, to environmentally friendly routes to biomass conversion, including the production of biofuels. The plant cell wall is a complex composite of cellulose microfibrils embedded in diverse polysaccharides collectively termed hemicelluloses. Xyloglucan is one such polysaccharide whose hydrolysis is catalyzed by diverse xyloglucanases. Here we present the structure of the Clostridium thermocellum xyloglucanase Xgh74A in both apo and ligand-complexed forms. The structures, in combination with mutagenesis data on the catalytic residues and the kinetics and specificity of xyloglucan hydrolysis reveal a complex subsite specificity accommodating seventeen monosaccharide moieties of the multibranched substrate in an open substrate binding terrain.",

keywords = "END-SPECIFIC CELLOBIOHYDROLASE, PLANT-CELL WALL, GLYCOSYL HYDROLASES, CELLULOSE SURFACES, EXPRESSION, CLONING, CLASSIFICATION, ENDOGLUCANASE, BIOSYNTHESIS, PURIFICATION",

author = "Carlos Martinez-Fleites and Guerreiro, {Catarina I. P. D.} and Baumann, {Martin J.} and Taylor, {Edward J.} and Prates, {Jose A. M.} and Ferreira, {Luis M. A.} and Fontes, {Carlos M. G. A.} and Harry Brumer and Davies, {Gideon J.}",

year = "2006",

month = aug,

day = "25",

doi = "10.1074/jbc.M603583200",

language = "English",

volume = "281",

pages = "24922--24933",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "34",

}

Martinez-Fleites, C, Guerreiro, CIPD, Baumann, MJ, Taylor, EJ, Prates, JAM, Ferreira, LMA, Fontes, CMGA, Brumer, H & Davies, GJ 2006, 'Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation', Journal of Biological Chemistry, vol. 281, no. 34, pp. 24922-24933. https://doi.org/10.1074/jbc.M603583200

Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation. / Martinez-Fleites, Carlos; Guerreiro, Catarina I. P. D.; Baumann, Martin J. et al.
In: Journal of Biological Chemistry, Vol. 281, No. 34, 25.08.2006, p. 24922-24933.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation

AU - Martinez-Fleites, Carlos

AU - Guerreiro, Catarina I. P. D.

AU - Baumann, Martin J.

AU - Taylor, Edward J.

AU - Prates, Jose A. M.

AU - Ferreira, Luis M. A.

AU - Fontes, Carlos M. G. A.

AU - Brumer, Harry

AU - Davies, Gideon J.

PY - 2006/8/25

Y1 - 2006/8/25

N2 - The enzymatic degradation of the plant cell wall is central both to the natural carbon cycle and, increasingly, to environmentally friendly routes to biomass conversion, including the production of biofuels. The plant cell wall is a complex composite of cellulose microfibrils embedded in diverse polysaccharides collectively termed hemicelluloses. Xyloglucan is one such polysaccharide whose hydrolysis is catalyzed by diverse xyloglucanases. Here we present the structure of the Clostridium thermocellum xyloglucanase Xgh74A in both apo and ligand-complexed forms. The structures, in combination with mutagenesis data on the catalytic residues and the kinetics and specificity of xyloglucan hydrolysis reveal a complex subsite specificity accommodating seventeen monosaccharide moieties of the multibranched substrate in an open substrate binding terrain.

AB - The enzymatic degradation of the plant cell wall is central both to the natural carbon cycle and, increasingly, to environmentally friendly routes to biomass conversion, including the production of biofuels. The plant cell wall is a complex composite of cellulose microfibrils embedded in diverse polysaccharides collectively termed hemicelluloses. Xyloglucan is one such polysaccharide whose hydrolysis is catalyzed by diverse xyloglucanases. Here we present the structure of the Clostridium thermocellum xyloglucanase Xgh74A in both apo and ligand-complexed forms. The structures, in combination with mutagenesis data on the catalytic residues and the kinetics and specificity of xyloglucan hydrolysis reveal a complex subsite specificity accommodating seventeen monosaccharide moieties of the multibranched substrate in an open substrate binding terrain.

KW - END-SPECIFIC CELLOBIOHYDROLASE

KW - PLANT-CELL WALL

KW - GLYCOSYL HYDROLASES

KW - CELLULOSE SURFACES

KW - EXPRESSION

KW - CLONING

KW - CLASSIFICATION

KW - ENDOGLUCANASE

KW - BIOSYNTHESIS

KW - PURIFICATION

U2 - 10.1074/jbc.M603583200

DO - 10.1074/jbc.M603583200

M3 - Article

SN - 0021-9258

VL - 281

SP - 24922

EP - 24933

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 34

ER -